ID A0A0Q6YW21_9BRAD Unreviewed; 249 AA.
AC A0A0Q6YW21;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=ASC80_21715 {ECO:0000313|EMBL:KQW18059.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW18059.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW18059.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18059.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW18059.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW18059.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQW18059.1}.
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DR EMBL; LMDP01000005; KQW18059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6YW21; -.
DR STRING; 1736436.ASC80_21715; -.
DR Proteomes; UP000051348; Unassembled WGS sequence.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR CDD; cd03023; DsbA_Com1_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR041205; ScsC_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF01323; DSBA; 1.
DR Pfam; PF18312; ScsC_N; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000051348}.
FT DOMAIN 58..246
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 249 AA; 27295 MW; 59B14A7521CAF68F CRC64;
MPLVLVSAAA AWLAFDPGFR RQQTANLSTG APNDEFERRV HDYLMAHPDV IMQSVNQLEA
RQRAKDETEV QAIVKSRADE IFRDAATPVS GNVDGDITLV EFFDYNCPYC RQVASVVTKA
EESDPKLRVA YKEFPILGPN SIVAAKAALA ANKQGKYVAF HRALYEVHGA VDSGKVKEVA
AAVGLDMDRL NADMKDPAIE ALIAKNFALA QALRINGTPG FVVGDQILRG ATDLKTLQTM
IRTAREHRQ
//
